ID A0A0D6AFK4_9CHRO Unreviewed; 1014 AA.
AC A0A0D6AFK4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN ORFNames=GM3708_1979 {ECO:0000313|EMBL:BAQ61573.1};
OS Geminocystis sp. NIES-3708.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Geminocystis.
OX NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ61573.1, ECO:0000313|Proteomes:UP000060542};
RN [1] {ECO:0000313|EMBL:BAQ61573.1, ECO:0000313|Proteomes:UP000060542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ61573.1,
RC ECO:0000313|Proteomes:UP000060542};
RA Hirose Y.;
RT "Geminocystis sp. NIES-3708 complete genome sequence.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00595};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR EMBL; AP014815; BAQ61573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6AFK4; -.
DR STRING; 1615909.GM3708_1979; -.
DR KEGG; gee:GM3708_1979; -.
DR PATRIC; fig|1615909.3.peg.2012; -.
DR Proteomes; UP000060542; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW Pyruvate {ECO:0000313|EMBL:BAQ61573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060542}.
FT ACT_SITE 191
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 661
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1014 AA; 116869 MW; A2D9252814696228 CRC64;
MTSAMTNYTE ELSIYSSSEL LLRHRLKLVE NLWESVLTNE CGQELVDLLD KLKSACSPEG
QTNETQNISV SKWIEQLELD DAIKAVRAFA LYFQLINIVE QHYEQRTQKL IRRTTTEDQV
NAIQKPESHN HQPTTLDTKE EAQSYFNPKS NPASGGTFHW LFPYLQKLNM PPPKIQQLLD
QLDINLVFTA HPTEIVRHTI RKKQRRISHF LEKLDAAEES FRAMGLTNSW EAENYRECLT
EEVRLWWRTD ELHQFKPTVL DEVDYALHYF QEVLFQTLPE LSIRLKQALH NTFPKLKSPT
HKFCYFGSWV GGDRDGNPFV TPEVTWSTAC YQRNLVIDKY LESMGQLNDI LSLSLHWCNV
MPELLDSLER DRIGMPELYD KLYVRYRQEP YRLKLAYIEQ RLKNTQVRNE ALSDPETRKS
IKLANKDDSL YPSKLDLLED LNLIKYNLEN TGLKCKELDH LISQVEIFGF HLTPLDFRQD
SSRHSDALSE IAEYLGVLDK PYEELSETEK TAWLVQELKT RRPLIPSEIN FSDATGETIE
TFKILRALQT EFGLDICHTY IISMTNYVSD VLEVLLLAKE AGLYDPILGI TSIRIVPLFE
TVEDLKRAPM VMTELFELPL YRACLAGGYE NVAKLPSNLV LPELNPKNLQ EIMLGYSDSN
KDSGFLSSNW EIHKAQKTLA RIGDKYGFNI KIFHGRGGSV GRGGGPAYAA ILAQPTSTID
GRIKITEQGE VLASKYSLPE LALYNLETIS TAVIQASLLG SGFDDIEPWN QIMEEIAAYS
RKAYRQLIYE QPDFIDFFLS VTPIEEISKL QISSRPARRS SGKKDISSLR AIPWVFSWTQ
SRFLLPAWYG VGTALQEFLN QEPEENLKLL RYFYLKWPFF KMVISKAEMT LSKVDLQMAS
HYVDELAKDE DKERFQKVFN QIAKEYYLSR DIVLQINEQE RLLDNDPELQ RSVQLRNGTI
VPLGFLQVSL LKRLRQYASQ DKAGLIHFRY SKEELLRGAL LTINGIAAGM RNTG
//